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PDBsum entry 1gpm
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Transferase (glutamine amidotransferase) PDB id
1gpm

 

 

 

 

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Contents
Protein chains
501 a.a. *
Ligands
PO4 ×4
POP ×4
AMP ×4
CIT ×4
Metals
_MG ×3
Waters ×790
* Residue conservation analysis
PDB id:
1gpm
Name: Transferase (glutamine amidotransferase)
Title: Escherichia coli gmp synthetase complexed with amp and pyrophosphate
Structure: Gmp synthetase. Chain: a, b, c, d. Synonym: xmp aminase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: guaa. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: tac promoter
Biol. unit: Tetramer (from PQS)
Resolution:
2.20Å     R-factor:   0.174    
Authors: J.J.G.Tesmer
Key ref: J.J.Tesmer et al. (1996). The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat Struct Biol, 3, 74-86. PubMed id: 8548458
Date:
04-Apr-95     Release date:   29-Jan-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04079  (GUAA_ECOLI) -  GMP synthase [glutamine-hydrolyzing] from Escherichia coli (strain K12)
Seq:
Struc: 		 
Seq:
Struc: 		525 a.a.
501 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.5.2  - Gmp synthase (glutamine-hydrolyzing).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		AMP and GMP Biosynthesis
      Reaction: XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP + diphosphate + 2 H+
XMP
 + L-glutamine
 + ATP
 + H2O
 =
GMP
Bound ligand (Het Group name = AMP)
corresponds exactly 		+
L-glutamate
Bound ligand (Het Group name = POP)
corresponds exactly 		+ AMP
 + diphosphate
 + 2 × H(+)
Bound ligand (Het Group name = CIT)
matches with 64.29% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Nat Struct Biol 3:74-86 (1996)
PubMed id: 8548458  
 
 
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
J.J.Tesmer, T.J.Klem, M.L.Deras, V.J.Davisson, J.L.Smith.
 
  ABSTRACT  
 
The crystal structure of GMP synthetase serves as a prototype for two families of metabolic enzymes. The Class I glutamine amidotransferase domain of GMP synthetase is found in related enzymes of the purine, pyrimidine, tryptophan, arginine, histidine and folic acid biosynthetic pathways. This domain includes a conserved Cys-His-Glu triad and is representative of a new family of enzymes that use a catalytic triad for enzymatic hydrolysis. The structure and conserved sequence fingerprint of the nucleotide-binding site in a second domain of GMP synthetase are common to a family of ATP pyrophosphatases, including NAD synthetase, asparagine synthetase and argininosuccinate synthetase.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19834552 F.Sarkari, T.Sanchez-Alcaraz, S.Wang, M.N.Holowaty, Y.Sheng, and L.Frappier (2009).
EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication.
  PLoS Pathog, 5, e1000624.  
19270703 N.LaRonde-LeBlanc, M.Resto, and B.Gerratana (2009).
Regulation of active site coupling in glutamine-dependent NAD(+) synthetase.
  Nat Struct Mol Biol, 16, 421-429.
PDB code: 3dla
18294973 D.Iwata-Reuyl (2008).
An embarrassment of riches: the enzymology of RNA modification.
  Curr Opin Chem Biol, 12, 126-133.  
18458150 E.J.Hart, and S.G.Powers-Lee (2008).
Mutation analysis of carbamoyl phosphate synthetase: does the structurally conserved glutamine amidotransferase triad act as a functional dyad?
  Protein Sci, 17, 1120-1128.  
18668122 Y.Ikeuchi, K.Kitahara, and T.Suzuki (2008).
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  EMBO J, 27, 2194-2203.  
17269935 E.L.Ang, J.P.Obbard, and H.Zhao (2007).
Probing the molecular determinants of aniline dioxygenase substrate specificity by saturation mutagenesis.
  FEBS J, 274, 928-939.  
17893083 J.R.Davies, R.M.Jackson, K.V.Mardia, and C.C.Taylor (2007).
The Poisson Index: a new probabilistic model for protein ligand binding site similarity.
  Bioinformatics, 23, 3001-3008.  
17512708 M.J.Wagemaker, D.C.Eastwood, C.van der Drift, M.S.Jetten, K.Burton, L.J.Van Griensven, and H.J.Op den Camp (2007).
Argininosuccinate synthetase and argininosuccinate lyase: two ornithine cycle enzymes from Agaricus bisporus.
  Mycol Res, 111, 493-502.  
18073113 M.Kuratani, Y.Yoshikawa, Y.Bessho, K.Higashijima, T.Ishii, R.Shibata, S.Takahashi, K.Yutani, and S.Yokoyama (2007).
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PDB codes: 2e21 2e89
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Mechanism-of-action determination of GMP synthase inhibitors and target validation in Candida albicans and Aspergillus fumigatus.
  Chem Biol, 14, 1163-1175.  
17951049 S.Mouilleron, and B.Golinelli-Pimpaneau (2007).
Conformational changes in ammonia-channeling glutamine amidotransferases.
  Curr Opin Struct Biol, 17, 653-664.  
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  Protein J, 25, 483-491.  
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Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites.
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Molecular dynamics simulations of a helicase.
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Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms: stereochemistry of the catalytic reaction.
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Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency.
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12621151 P.M.Quigley, K.Korotkov, F.Baneyx, and W.G.Hol (2003).
The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad.
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12799468 R.Amaro, E.Tajkhorshid, and Z.Luthey-Schulten (2003).
Developing an energy landscape for the novel function of a (beta/alpha)8 barrel: ammonia conduction through HisF.
  Proc Natl Acad Sci U S A, 100, 7599-7604.  
11839304 A.Douangamath, M.Walker, S.Beismann-Driemeyer, M.C.Vega-Fernandez, R.Sterner, and M.Wilmanns (2002).
Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex.
  Structure, 10, 185-193.
PDB codes: 1gpw 1k9v
11756425 A.Saeed-Kothe, and S.G.Powers-Lee (2002).
Specificity determining residues in ammonia- and glutamine-dependent carbamoyl phosphate synthetases.
  J Biol Chem, 277, 7231-7238.  
11809762 C.T.Lemke, and P.L.Howell (2002).
Substrate induced conformational changes in argininosuccinate synthetase.
  J Biol Chem, 277, 13074-13081.
PDB codes: 1kp2 1kp3
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Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate.
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PDB code: 1l9x
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Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia.
  J Biol Chem, 277, 39722-39727.
PDB code: 1m6v
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Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA.
  Proteins, 48, 1.  
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Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action.
  J Biol Chem, 277, 15890-15896.
PDB codes: 1kh1 1kh2 1kor
12360532 S.Korolev, T.Skarina, E.Evdokimova, S.Beasley, A.Edwards, A.Joachimiak, and A.Savchenko (2002).
Crystal structure of glutamine amidotransferase from Thermotoga maritima.
  Proteins, 49, 420-422.
PDB code: 1kxj
11371633 G.Spraggon, C.Kim, X.Nguyen-Huu, M.C.Yee, C.Yanofsky, and S.E.Mills (2001).
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
  Proc Natl Acad Sci U S A, 98, 6021-6026.
PDB codes: 1i7q 1i7s
  11380987 H.C.Pace, and C.Brenner (2001).
The nitrilase superfamily: classification, structure and function.
  Genome Biol, 2, REVIEWS0001.  
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The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily.
  Proteins, 42, 230-236.  
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Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site.
  Proc Natl Acad Sci U S A, 98, 11169-11174.
PDB code: 1ie0
11160884 N.V.Grishin (2001).
KH domain: one motif, two folds.
  Nucleic Acids Res, 29, 638-643.  
11208798 T.J.Klem, Y.Chen, and V.J.Davisson (2001).
Subunit interactions and glutamine utilization by Escherichia coli imidazole glycerol phosphate synthase.
  J Bacteriol, 183, 989-996.  
11395405 X.Huang, H.M.Holden, and F.M.Raushel (2001).
Channeling of substrates and intermediates in enzyme-catalyzed reactions.
  Annu Rev Biochem, 70, 149-180.  
10850988 A.K.Bera, S.Chen, J.L.Smith, and H.Zalkin (2000).
Temperature-dependent function of the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel and coupling with glycinamide ribonucleotide synthetase in a hyperthermophile.
  J Bacteriol, 182, 3734-3739.  
11080634 C.E.Stevenson, F.Sargent, G.Buchanan, T.Palmer, and D.M.Lawson (2000).
Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution.
  Structure, 8, 1115-1125.
PDB code: 1e5k
10713991 K.A.Denessiouk, and M.S.Johnson (2000).
When fold is not important: a common structural framework for adenine and AMP binding in 12 unrelated protein families.
  Proteins, 38, 310-326.  
10852731 M.A.Rishavy, W.W.Cleland, and C.J.Lusty (2000).
15N isotope effects in glutamine hydrolysis catalyzed by carbamyl phosphate synthetase: evidence for a tetrahedral intermediate in the mechanism.
  Biochemistry, 39, 7309-7315.  
10966576 M.Y.Galperin, and N.V.Grishin (2000).
The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase.
  Proteins, 41, 238-247.  
10722656 P.M.Palenchar, C.J.Buck, H.Cheng, T.J.Larson, and E.G.Mueller (2000).
Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate.
  J Biol Chem, 275, 8283-8286.  
11114201 X.Du, I.G.Choi, R.Kim, W.Wang, J.Jancarik, H.Yokota, and S.H.Kim (2000).
Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.
  Proc Natl Acad Sci U S A, 97, 14079-14084.
PDB code: 1g2i
  10338021 B.Zhang, L.Rychlewski, K.Pawłowski, J.S.Fetrow, J.Skolnick, and A.Godzik (1999).
From fold predictions to function predictions: automation of functional site conservation analysis for functional genome predictions.
  Protein Sci, 8, 1104-1115.  
10508782 C.H.Weber, Y.S.Park, S.Sanker, C.Kent, and M.L.Ludwig (1999).
A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis.
  Structure, 7, 1113-1124.
PDB code: 1coz
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Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis.
  Protein Sci, 8, 2424-2427.  
10387030 F.M.Raushel, J.B.Thoden, and H.M.Holden (1999).
The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia.
  Biochemistry, 38, 7891-7899.  
10587438 J.B.Thoden, X.Huang, F.M.Raushel, and H.M.Holden (1999).
The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway.
  Biochemistry, 38, 16158-16166.
PDB codes: 1c30 1c3o 1cs0
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PDB code: 1qdl
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Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
  Biochemistry, 38, 16146-16157.
PDB code: 1ct9
9858783 A.Hewagama, H.I.Guy, M.Chaparian, and D.R.Evans (1998).
The function of Glu338 in the catalytic triad of the carbamoyl phosphate synthetase amidotransferase domain.
  Biochim Biophys Acta, 1388, 489-499.  
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Carbamoyl phosphate synthetase: a crooked path from substrates to products.
  Curr Opin Chem Biol, 2, 624-632.  
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Carbamoyl phosphate synthetase: a tunnel runs through it.
  Curr Opin Struct Biol, 8, 679-685.  
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Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis.
  Biochemistry, 37, 8825-8831.
PDB code: 1a9x
9914248 J.L.Smith (1998).
Glutamine PRPP amidotransferase: snapshots of an enzyme in action.
  Curr Opin Struct Biol, 8, 686-694.  
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Reactivity of selenomethionine--dents in the magic bullet?
  Structure, 6, 815-819.  
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A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure.
  Structure, 6, 1129-1140.
PDB code: 2nsy
  9620974 R.Cantoni, M.Branzoni, M.Labò, M.Rizzi, and G.Riccardi (1998).
The MTCY428.08 gene of Mycobacterium tuberculosis codes for NAD+ synthetase.
  J Bacteriol, 180, 3218-3221.  
  9827998 W.M.Liu, and K.C.Chou (1998).
Singular points of protein beta-sheets.
  Protein Sci, 7, 2324-2330.  
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Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.
  Structure, 5, 895-906.
PDB code: 1sur
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Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product.
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Expression, purification, mass spectrometry, crystallization and multiwavelength anomalous diffraction of selenomethionyl PvuII DNA methyltransferase (cytosine-N4-specific).
  Eur J Biochem, 247, 1009-1018.  
8910338 B.Xiang, and G.D.Markham (1996).
The conformation of inosine 5'-monophosphate (IMP) bound to IMP dehydrogenase determined by transferred nuclear overhauser effect spectroscopy.
  J Biol Chem, 271, 27531-27535.  
8663035 J.H.Kim, J.M.Krahn, D.R.Tomchick, J.L.Smith, and H.Zalkin (1996).
Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site.
  J Biol Chem, 271, 15549-15557.
PDB code: 1ecg
8805567 M.N.Isupov, G.Obmolova, S.Butterworth, M.A.Badet-Denisot, B.Badet, I.Polikarpov, J.A.Littlechild, and A.Teplyakov (1996).
Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase.
  Structure, 4, 801-810.
PDB codes: 1gdo 1gms 1xff 1xfg
  8895556 M.Rizzi, C.Nessi, A.Mattevi, A.Coda, M.Bolognesi, and A.Galizzi (1996).
Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis.
  EMBO J, 15, 5125-5134.
PDB code: 1nsy
8916230 M.Rizzi, C.Nessi, M.Bolognesi, A.Coda, and A.Galizzi (1996).
Crystallization of NAD+ synthetase from Bacillus subtilis.
  Proteins, 26, 236-238.  
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